Ontology highlight
ABSTRACT:
SUBMITTER: Che T
PROVIDER: S-EPMC7052193 | biostudies-literature | 2020 Mar
REPOSITORIES: biostudies-literature
Che Tao T English Justin J Krumm Brian E BE Kim Kuglae K Pardon Els E Olsen Reid H J RHJ Wang Sheng S Zhang Shicheng S Diberto Jeffrey F JF Sciaky Noah N Carroll F Ivy FI Steyaert Jan J Wacker Daniel D Roth Bryan L BL
Nature communications 20200302 1
Recent studies show that GPCRs rapidly interconvert between multiple states although our ability to interrogate, monitor and visualize them is limited by a relative lack of suitable tools. We previously reported two nanobodies (Nb39 and Nb6) that stabilize distinct ligand- and efficacy-delimited conformations of the kappa opioid receptor. Here, we demonstrate via X-ray crystallography a nanobody-targeted allosteric binding site by which Nb6 stabilizes a ligand-dependent inactive state. As Nb39 s ...[more]